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While the native function of the prion protein is not known
Playing with things they don't understand. Wasn't this thing created by feeding plant eaters (cows), meat (ground up sheep). So the answer must be to use genetic engineering, something else they don't fully understand, to fix the previous monstrous creation. Wow!
I know alarmist language is fun and all... especially here on ATS, but let's approach the topic with a scintilla of reason.
Originally posted by HimWhoHathAnEar
Sorry, don't have the faith in science you do. So I'll exercise my right to whatever language I feel like, thank you. Because, by the time 'science' makes a mistake, we may end up with something far worse than prions.
Protein infectious agent associated with several neurological diseases (scrapie; kuru; Creutzfeld-Jakob syndrome; Alzheimer's disease). Each disease has a different prion.
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Prion: A disease-causing agent that is neither bacterial nor fungal nor viral and contains no genetic material. A prion is a protein that occurs normally in a harmless form. By folding into an aberrant shape, the normal prion turns into a rogue agent. It then coopts other normal prions to become rogue prions.
Prions have been held responsible for a number of degenerative brain diseases, including scrapie (a fatal disease of sheep and goats), mad cow disease, Creutzfeldt-Jacob disease, fatal familial insomnia, kuru, an unusual form of hereditary dementia known as Gertsmann-Straeussler-Scheinker disease, and possibly some cases of Alzheimer's disease.
Dr. Stanley B. Prusiner received the 1997 Nobel Prize in Physiology or Medicine for his discovery of prions. See also: Prusiner, Stanley B..
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prion (plural prions)
1. The etiologic agent of transmissible spongiform encephalopathies. The only self-replicating cause of disease known to lack nucleic acids.
2. A self-propagating alternative conformer of any protein.
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prion - The word, for proteinaceous infectious agent, was coined in 1982 by neurologist Stanley Prusiner as part of a hypothesis regarding ailments bearing aetiologic resemblance to those caused by slow viruses (for instance, kuru). The hypothesis has been borne out by investigation. Prions are now believed responsible for several transmissible neurodegenerative diseases
...U.S. herd an ideal resource for companies that extract blood and other products from cattle for use in human pharmaceuticals.
...it may not be necessary for Hematech to use prion-free cattle as it strives to make potent, disease-killing antibodies in cattle for use in humans with life-threatening infections.
Misfolded prion proteins are blamed for BSE and other, similar brain diseases. It is known that certain genetic variations make animals more susceptible to the diseases.
Originally posted by HimWhoHathAnEar
We're not eating mice.
Nope but we (yourself included) are consuming large amounts of genetically modified corn, soy, and canola. So how is this so much different?
Originally posted by soficrow
This is just marketing - a bs press releas.
Human drugs and vaccines are manufactured using U.S. cattle and cattle products.
Continued profitability, and avoiding liability lawsuits, depends on convincing people that the process is safe, always was safe, and always will be safe - that prion
diseases like Mad Cow are "genetic," only affect the brain, and are NOT a problem in the USA.
Who cares if there's a genetically engineered cow without the mutation on chromosome 20 that codes for 33–35 kD protein?
Drug and vaccine manufacturing processes don't just spread infectious prions - standard manufacturing processes create new infectious prion strains.
That's not the only infectious prion - in cattle, in vaccines or drugs, or infecting humans.
Genetic engineering does NOT solve the prion problem.
Originally posted by HimWhoHathAnEar
I didn't agree to eat that garbage either. So I guess while they're slipping it into the food supply anyway, might as well just let 'em keep goin' on to bigger and better things?
I'm not sure that that stuff isn't causing problems. There are unexplained increases in many diseases these days, so who's to say?
How is it so much different? I guess I just see a bigger difference between Plants and Animals than you do.
so who's to say?
Why would you be sure?
You've apparently not even read enough about the topic to be aware of the fact that you've been consuming GMO foods for what probably amounts to a good portion of your life.
Personally the issue of BSE is a non-issue for me...
Originally posted by HimWhoHathAnEar
I think you're making assumptions about my age and my knowledge. 'I' don't effect what 'they' get into the food supply, and I am aware of organic food.
This explains alot. Confidence may be easier to have in something that only effects others.
"What we are learning from both yeast and mammalian prions raises the disturbing possibility that the process of infecting, heat-rendering of the animal parts, and then re-infecting cows might actually have selected for a prion strain conformation that is particularly virulent and resistant to being inactivated," Weissman said. "So, it might have been this very process that humans set up that made the bovine prion so virulent and created the epidemic of mad cow disease."
kallikak
soficrow
This is just marketing - a bs press releas.
Well... it's technically a news report written about some research published in Nature Biotechnology. I doubt the scientists working on the project consider it "bs," but opinions do vary.
The USDA's Agricultural Research Service (ARS) announced Sunday that initial results of a research project involving prion-free cattle are now available online at www.nature.com/nbt/.
...The evaluation of the prion-free cattle was led by veterinary medical officer Juergen Richt of ARS' National Animal Disease Center in Ames, Iowa.
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Genetic Modification in Livestock
Prevention of BSE/TSE by Knockout of the Prion Gene
NIH Grant Abstract: Bovine spongiform encephalopathy is an emerging prion disease of cattle. Mounting evidence indicates that BSE is transmissible to humans in the form of a new, deadly variant of Creutzfeldt-Jakob disease (vCJD). Consumption of BSE-tainted beef has been implicated as the most likely mode of transmission. BSE thus represents a threat to human health via the food supply and other bovine-derived products. As no vaccine, diagnostic test or therapy exists for either vCJD or BSE, protection depends on preventative measures. The pathogenesis of prion disease requires expression of host-encoded prion protein. In mice, priori gene knockout of confers resistance to priori disease. Knockout of the prion gene in cattle should similarly render the bovine resistant to BSE. The long-term goal of this work is to test the hypothesis that cattle bearing bi-allelic prion knockouts are resistant to BSE. Offspring with mono-allelic prion knockouts will be bred in future work to generate cattle with bi-allelic prion knockouts.
NIH Grant Number: 1R21NS045908-01
PI Name: EYESTONE, WILLARD H.
Project Title: Generation of Prion Knockout Cattle
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Production of Human Antibodies in Cattle Blood
Hematech and Kirin
Human polyclonal antibodies (hPABs) are useful therapeutics, but because they are available only from human donors, their supply and application is limited. To address this need, we prepared a human artificial chromosome (HAC) vector containing the entire un-rearranged sequences of the human immunoglobulin (hIg) heavy-chain (H) and lambda (lambda) light-chain loci. The HAC vector was introduced into bovine primary fetal fibroblasts using a microcell-mediated chromosome transfer (MMCT) approach. Primary selection was carried out, and the cells were used to produce cloned bovine fetuses. Secondary selection was done on the regenerated fetal cell lines, which were then used to produce four healthy transchromosomic (Tc) calves. Human immunoglobulin proteins were detected in the blood of newborn calves. The production of Tc calves is an important step in the development of a system for producing therapeutic hPABs.
Nat Biotechnol. 2002 Sep;20(9):889-94.
Cloned transchromosomic calves producing human immunoglobulin.
Kuroiwa Y, Kasinathan P, Choi YJ, Naeem R, Tomizuka K, Sullivan EJ, Knott JG, Duteau A,
Goldsby RA, Osborne BA, Ishida I, Robl JM.
Pharmaceutical Research Laboratory, Kirin Brewery Co., Ltd., Japan.
Dr. Crick assumed from the start that the genetic code was universal to all forms of life. Dr. Crick formulated the "central dogma" -- the view that the usual sequence of events is from DNA to RNA to protein. By contrast, Dr. Prusiner has postulated the prion -- the idea that
proteins can go it alone. DNA and RNA are unnecessary to the prion.
The discovery that a small change in the condition of a cell can cause the development of a prion offers an explanation, says Prusiner, for the sporadic form of Creutzfeldt Jakob disease (CJD), which is responsible for 85 percent of cases of prion disease in humans (occurring in 1 or 2 people per million) and is believed to develop spontaneously. It also supports his belief, he says, that sporadic forms of prion disease are caused by prion strains that are different from the one causing bovine spongiform encephalopathy (BSE) in cattle in Britain.
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Recommendations for the Use of Vaccines Manufactured with Bovine-Derived Materials: Bovine-derived materials have traditionally been used in the manufacture of many biological products, including vaccines.
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The FDA's TSE Advisory Committee and Related Biological Products Advisory Committee met in 2000 to discuss the issue of potential risk of BSE from vaccines, talked about revealing the risks to parents and concluded, "We have a duty...to protect the vaccine system in this country." (PDF)
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The role of hydrophobicity patterns in prion folding
Prions' Changeability: Nuclear magnetic resonance shows more pieces of the puzzle
Fibril shape is the basis of prion strains and cross-species prion infection
Prion Yields Clues to Infection Across Species Barriers
Originally posted by soficrow
Just a tidbit from my files:
soficrow
The research was funded by the National Institutes of Health through Hematech, a biotechnology company and a South Dakota subsidiary of Kirin, who is interested in genetically engineering cows to produce antibiotics and other medicines for people- and was evaluated by the Agricultural Research Service of the USDA.
For years, the USDA's position on BSE and prions was, "Problem? What problem? Prions don't exist."
Now, they're saying, "No problem - we fixed it. We can genetically engineer cattle that are immune to prions."
Q: So why the dance? Why fund research, and evaluate it as successful, while saying it's not really needed?
A: Because the USDA is in the business of protecting the US cattle industry - NOT public health.
Originally posted by soficrow
Never mind the food supply - this is more about "biological products." The US being the primary supplier of bovine-derived materials to the drug and biotech industries.
And: The US market position hinges on the assumption that US cattle are prion-free. The USDA is concerned first with protecting the nation's cattle industry - so research supported by the department can be seen as designed to support the industry - and "research reports" can be seen as press releases and marketing tools.
Q: Can genetic modification prevent prion diseases?
A: Only if genes are required to make prions. They're not.
Dr. Crick assumed from the start that the genetic code was universal to all forms of life. Dr. Crick formulated the "central dogma" -- the view that the usual sequence of events is from DNA to RNA to protein. By contrast, Dr. Prusiner has postulated the prion -- the idea that proteins can go it alone. DNA and RNA are unnecessary to the prion.
The discovery that a small change in the condition of a cell can cause the development of a prion offers an explanation, says Prusiner, for the sporadic form of Creutzfeldt Jakob disease (CJD), which is responsible for 85 percent of cases of prion disease in humans (occurring in 1 or 2 people per million) and is believed to develop spontaneously. It also supports his belief, he says, that sporadic forms of prion disease are caused by prion strains that are different from the one causing bovine spongiform encephalopathy (BSE) in cattle in Britain.
Bovine-derived materials have traditionally been used in the manufacture of many biological products, including vaccines.
The FDA's TSE Advisory Committee and Related Biological Products Advisory Committee met in 2000 to discuss the issue of potential risk of BSE from vaccines, talked about revealing the risks to parents and concluded, "We have a duty...to protect the vaccine system in this country."
The role of hydrophobicity patterns in prion folding
Prions' Changeability: Nuclear magnetic resonance shows more pieces of the puzzle
Fibril shape is the basis of prion strains and cross-species prion infection
Prion Yields Clues to Infection Across Species Barriers
Developing "BSE prion-free cattle" now is like closing the barn door after the cows already escaped, and left town. On a full plane.
PS. If you clicked on the Kirin link above, you may be wondering why a Japanese brewery is interested in prions. Hint: Brewing beer involves using yeast. (Yeast carries prions. Lots of different strains.)
1997: Researchers for some time have been able to create proteins in the lab by stringing together amino acids, but this has been a very hit-and-miss process because of the vast number of ways that the 20 amino acids found in nature can go together.
***
Computational Protein Design / Protein-Protein Interactions / Structural Biology / Ubiquitination
What is protein design? Most ambitiously it is the creation of novel proteins to perform useful tasks. At a more modest level it might be identifying amino acid mutations that enhance protein stability, alter binding specificity, or increase solubility.
How do we design proteins? We have developed a computer program that identifies low energy sequences for a target structure or interface. In essence, it is like solving a jigsaw puzzle.The pieces, in this case amino acids, must fit together so that there are no overlaps and little empty space.In addition, specific interactions such as hydrogen bonds must be satisfied..
What have we designed in the past? In the past we have used our program to enhance protein stability, design a protein with a topology that has not been observed in nature, enhance protein-protein binding affinities and design a protein conformational switch..
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NASA Scientists Create Amino Acids in Deep-Space-Like Environment
A team of scientists at the NASA Astrochemistry Laboratory today announced that they had created amino acids in conditions mimicking deep space. Amino acids are the basic components of proteins, from which all life is made. According to researcher Max Bernstein, "We found that amino acids can be made in the dense interstellar clouds where planetary systems and stars are made. Our experiments suggest that amino acids should be everywhere, wherever there are stars and planets."
The three amino acids produced in the Astrochemistry Lab are similar to those found previously in certain meteorites. Meteorites are pieces of asteroids or comets. The chemical similarities may indicate that amino acids were made in deep space, before the solar system formed, then eventually fell to Earth in meteorites. "This finding suggests that Earth may have been seeded with amino acids from space in its earliest days," said team member Jason Dworkin, adding, "[T]his increases the odds that life also evolved in places other than Earth."
In their deep-space simulator, the Astrochemistry Lab team has previously produced cell-membrane-like structures and other organic compounds basic to life. Next, they plan to investigate why left- and right-handed amino acids exist in space, but only the left-handed forms are used by life on Earth. Other scientists on the team include Lou Allamandola, George Cooper and Scott Sandford.
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Chemical synthesis of proteins
Chemical synthesis is the most powerful approach for constructing proteins of novel design and structure, allowing for variation of covalent structure without limitations. Here we describe the various chemical methods that are currently used for creating proteins of unique architecture and function.
***
Patch engineering: a general approach for creating proteins that have new binding activities.
Patch engineering is a technique for creating folded proteins that have new binding activities. Different protein scaffolds are used to present a patch of discontinuous residues on a folded-protein surface. By varying simultaneously the residues in these patches and displaying these mutant proteins on phage, one can select proteins that have new binding activities. Patch engineering is applicable to any protein fold. Novel proteins derived by this approach might replace antibodies in certain applications or provide lead molecules for the design of non-peptide analogues.
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Creating Proteins
***
An efficient method for generating proteins
...bacteria lacking RRF cannot exist because of their inability to create new proteins.
'Synthetic Life' Created in Labs
New synthetic amino acid developed by UCI Chemists
Originally posted by soficrow
You're all over the place kallikak, without sources or references. So I'll just tackle your main assumptions.
You say DNA is required to create proteins.
Yet proteins routinely are created in labs, by human scientists,
and DNA-coded proteins are changed, also routinely. Purposefully and accidentally.
Are you saying humans can create proteins without DNA, and change DNA-coded proteins, but nature (or God) cannot?
Some old news:
1997: Researchers for some time have been able to create proteins in the lab by stringing together amino acids, but this has been a very hit-and-miss process because of the vast number of ways that the 20 amino acids found in nature can go together.
Computational Protein Design / Protein-Protein Interactions / Structural Biology / Ubiquitination
What is protein design? Most ambitiously it is the creation of novel proteins to perform useful tasks. At a more modest level it might be identifying amino acid mutations that enhance protein stability, alter binding specificity, or increase solubility.
How do we design proteins? We have developed a computer program that identifies low energy sequences for a target structure or interface. In essence, it is like solving a jigsaw puzzle.The pieces, in this case amino acids, must fit together so that there are no overlaps and little empty space.In addition, specific interactions such as hydrogen bonds must be satisfied..
What have we designed in the past? In the past we have used our program to enhance protein stability, design a protein with a topology that has not been observed in nature, enhance protein-protein binding affinities and design a protein conformational switch.